SitesBLAST
Comparing 6939292 FitnessBrowser__SB2B:6939292 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P21213 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Rattus norvegicus (Rat) (see paper)
37% identity, 89% coverage: 1:462/518 of query aligns to 103:566/657 of P21213
- S254 (= S153) mutation to A: Complete loss of activity.
B2J528 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
34% identity, 99% coverage: 1:511/518 of query aligns to 18:547/569 of B2J528
- A167 (= A152) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S153) modified: 2,3-didehydroalanine (Ser)
- G169 (= G154) modified: Crosslink with 167, 5-imidazolinone (Ala-Gly)
Q3M5Z3 Phenylalanine ammonia-lyase; EC 4.3.1.24 from Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) (see 2 papers)
33% identity, 97% coverage: 11:511/518 of query aligns to 25:547/567 of Q3M5Z3
- L108 (≠ H93) mutation to A: Slightly decreases catalytic rate.; mutation to G: Decreases catalytic rate.
- A167 (= A152) modified: Crosslink with 169, 5-imidazolinone (Ala-Gly)
- S168 (= S153) modified: 2,3-didehydroalanine (Ser)
- G169 (= G154) modified: Crosslink with 167, 5-imidazolinone (Ala-Gly)
- C503 (= C470) mutation to S: Prevents formation of artifactual disulfide bonds and increases solubility; when associated with S-565.
Sites not aligning to the query:
- 1:21 mutation Missing: No effect on enzyme activity.
- 565 C→S: Prevents formation of artifactual disulfide bonds and increases solubility; when associated with S-503.
Q20502 Histidine ammonia-lyase; Histidase; EC 4.3.1.3 from Caenorhabditis elegans (see paper)
35% identity, 96% coverage: 17:515/518 of query aligns to 135:630/677 of Q20502
- D536 (≠ F416) mutation to N: In am130; causes strong resistance to nickel and zinc toxicity.
P0DO55 Phenylalanine/tyrosine ammonia-lyase 1; FuPAL1; EC 4.3.1.25 from Fritillaria unibracteata (Sichuan fritillary) (see paper)
33% identity, 92% coverage: 9:487/518 of query aligns to 60:551/722 of P0DO55
- F141 (= F92) mutation to H: Increased activity toward L-tyrosine (L-Tyr) but reduced ability to use L-phenylalanine (L-Phe) as substrate.
- S208 (≠ A152) mutation to A: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- I218 (≠ L162) mutation to P: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
- E490 (= E421) mutation to N: Higher binding affinity for L-phenylalanine (L-Phe) and decrease catalytic efficiency.
5ltmB Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis (y78f-c503s-c565s) bound to cinnamate (see paper)
32% identity, 97% coverage: 11:511/518 of query aligns to 1:521/537 of 5ltmB
- active site: F54 (≠ Y63), G61 (= G70), L84 (≠ H93), N197 (= N205), Y288 (= Y286), R291 (= R289), F337 (= F335), Q426 (= Q425)
- binding hydrocinnamic acid: F60 (≠ Y69), A143 (= A152), L145 (= L156), Y288 (= Y286), R291 (= R289)
Q6GZ04 Phenylalanine aminomutase (L-beta-phenylalanine forming); Phenylalanine ammonia-lyase; EC 5.4.3.10; EC 4.3.1.24 from Taxus canadensis (Canadian yew) (see paper)
32% identity, 96% coverage: 1:496/518 of query aligns to 17:525/698 of Q6GZ04
- Y80 (= Y63) mutation to F: Abolishes enzyme activity.
- L104 (= L89) mutation to A: Decreases enzyme activity.
- Q319 (= Q283) binding
- R325 (= R289) binding
Q68G84 Phenylalanine aminomutase (L-beta-phenylalanine forming); Phenylalanine ammonia-lyase; EC 5.4.3.10; EC 4.3.1.24 from Taxus chinensis (Chinese yew) (Taxus wallichiana var. chinensis) (see 2 papers)
32% identity, 96% coverage: 1:496/518 of query aligns to 17:525/687 of Q68G84
- Y80 (= Y63) active site, Proton donor/acceptor; mutation Y->A,F: Abolishes enzyme activity.
- A175 (= A152) modified: Crosslink with 177, 5-imidazolinone (Ala-Gly)
- S176 (= S153) modified: 2,3-didehydroalanine (Ser)
- G177 (= G154) modified: Crosslink with 175, 5-imidazolinone (Ala-Gly)
- N231 (= N205) binding ; mutation to A: Abolishes the formation of the MIO cofactor and thereby abolishes enzyme activity.; mutation to X: Abolishes enzyme activity; when associated with X-355.
- Q319 (= Q283) binding ; mutation to M: Increases deamination activity with beta-Phe. Increases beta-regioselectivity in the amination of cinnamate. Abolishes enzyme activity; when associated with K-325.
- Y322 (= Y286) mutation to A: Abolishes the formation of the MIO cofactor and thereby abolishes enzyme activity.; mutation to X: Abolishes enzyme activity; when associated with X-371.
- R325 (= R289) binding ; mutation to K: Increases deamination activity with beta-Phe. Increases beta-regioselectivity in the amination of cinnamate. Abolishes enzyme activity; when associated with M-319.
- N355 (= N319) binding ; mutation to X: Abolishes enzyme activity; when associated with X-231.
- F371 (= F335) mutation to X: Abolishes enzyme activity; when associated with X-322.
- N458 (= N424) binding
Q0VZ68 Tyrosine 2,3-aminomutase; Tyrosine ammonia-lyase; EC 5.4.3.6; EC 4.3.1.23 from Chondromyces crocatus (see paper)
34% identity, 84% coverage: 62:498/518 of query aligns to 50:498/531 of Q0VZ68
- F57 (≠ Y69) mutation to Y: Loss of aminomutase activity.
- LVPVMI 60:65 (≠ SCTVTV 72:77) mutation to MIYMLV: Shift towards ammonia lyase activity.
- RSHA 79:82 (≠ RFHG 91:94) mutation to TFLS: Total loss of aminomutase activity.
- RSHAA 79:83 (≠ RFHGC 91:95) mutation to YHLAT: Total loss of aminomutase activity.
- G184 (≠ R196) mutation to R: Gain of aminomutase activity.
- K242 (= K254) mutation to R: Gain of aminomutase activity.
- 275:288 (vs. 278:279, 0% identical) mutation Missing: Total loss of aminomutase activity.
- P377 (= P368) mutation to R: No effect.
- C396 (≠ H390) mutation to S: No effect.
- E399 (≠ K393) mutation to A: Loss of aminomutase activity and increased product racemization. Gain of ammonia-lyase activity.; mutation to K: Loss of aminomutase and ammonia-lyase activity. Higher enantiomeric excess of (R)-beta-tyrosine.; mutation to M: Loss of aminomutase and ammonia-lyase activity.
- 399:406 (vs. 393:400, 13% identical) mutation to MIAQVTSA: Residual aminomutase activity.
- 427:433 (vs. 421:427, 43% identical) mutation to SAGREDH: Total loss of aminomutase activity.; mutation to SANQEDH: Total loss of aminomutase activity.
Q8GMG0 MIO-dependent tyrosine 2,3-aminomutase; Tyrosine ammonia-lyase; EC 5.4.3.6; EC 4.3.1.23 from Streptomyces globisporus (see 3 papers)
34% identity, 96% coverage: 19:514/518 of query aligns to 20:526/539 of Q8GMG0
- Y63 (= Y63) active site, Proton donor/acceptor; mutation to F: Complete loss of activity. It does not affect the over-all structure of the enzyme.
- E71 (≠ D71) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- H93 (= H93) binding ; mutation to F: Complete loss of activity.
- A152 (= A152) modified: Crosslink with 154, 5-imidazolinone (Ala-Gly)
- S153 (= S153) modified: 2,3-didehydroalanine (Ser)
- G154 (= G154) modified: Crosslink with 152, 5-imidazolinone (Ala-Gly)
- N205 (= N205) binding
- Y303 (≠ R281) mutation to A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine.
- R311 (= R289) binding
- Y415 (≠ I397) mutation to V: Complete loss of activity.
P24481 Phenylalanine ammonia-lyase 1; EC 4.3.1.24 from Petroselinum crispum (Parsley) (Petroselinum hortense) (see paper)
32% identity, 92% coverage: 9:487/518 of query aligns to 54:545/716 of P24481
- S203 (= S153) modified: 2,3-didehydroalanine (Ser); mutation to A: Complete loss of activity.
- S210 (= S160) mutation to A: No loss of activity.
4c5sC Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from taxus chinensis (see paper)
31% identity, 96% coverage: 1:496/518 of query aligns to 9:507/642 of 4c5sC
- active site: A71 (≠ Y63), G78 (= G70), L99 (≠ H93), N213 (= N205), Y304 (= Y286), R307 (= R289), F353 (= F335), Q441 (= Q425)
- binding (3S)-3-amino-2,2-difluoro-3-phenylpropanoic acid: G78 (= G70), G159 (= G154), L161 (= L156), N213 (= N205), Y304 (= Y286), R307 (= R289), N337 (= N319), F353 (= F335), E437 (= E421)
3unvA Pantoea agglomerans phenylalanine aminomutase (see paper)
33% identity, 82% coverage: 40:463/518 of query aligns to 30:467/514 of 3unvA
- active site: Y53 (= Y63), G60 (= G70), V83 (≠ H93), L191 (= L203), D291 (= D284), S294 (= S287), G340 (= G333), D427 (≠ H423)
- binding phenylalanine: Y53 (= Y63), G60 (= G70), G142 (= G154), L144 (= L156), N326 (= N319), F342 (= F335)
- binding (3S)-3-amino-3-phenylpropanoic acid: Y53 (= Y63), G60 (= G70), G142 (= G154), N193 (= N205), N326 (= N319), F342 (= F335)
2rjsA Sgtam bound to substrate mimic (see paper)
34% identity, 96% coverage: 19:514/518 of query aligns to 9:513/526 of 2rjsA
- active site: Y52 (= Y63), G59 (= G70), H82 (= H93), N192 (= N205), Y295 (= Y286), R298 (= R289), F343 (= F335), Q429 (= Q425)
- binding (3R)-3-amino-2,2-difluoro-3-(4-methoxyphenyl)propanoic acid: Y52 (= Y63), G59 (= G70), H82 (= H93), G141 (= G154), L143 (= L156), N192 (= N205), Y295 (= Y286), R298 (= R289), F343 (= F335), Q429 (= Q425)
2rjrA Substrate mimic bound to sgtam (see paper)
34% identity, 96% coverage: 19:514/518 of query aligns to 9:513/526 of 2rjrA
- active site: Y52 (= Y63), G59 (= G70), H82 (= H93), N192 (= N205), Y295 (= Y286), R298 (= R289), F343 (= F335), Q429 (= Q425)
- binding (2S,3S)-3-(4-fluorophenyl)-2,3-dihydroxypropanoic acid: Y52 (= Y63), G59 (= G70), H82 (= H93), G141 (= G154), L143 (= L156), N192 (= N205), F343 (= F335), Q429 (= Q425)
2qveA Crystal structure of sgtam bound to mechanism based inhibitor (see paper)
34% identity, 96% coverage: 19:514/518 of query aligns to 9:513/526 of 2qveA
- active site: Y52 (= Y63), G59 (= G70), H82 (= H93), N192 (= N205), Y295 (= Y286), R298 (= R289), F343 (= F335), Q429 (= Q425)
- binding (3R)-3-amino-2,2-difluoro-3-(4-hydroxyphenyl)propanoic acid: Y52 (= Y63), G59 (= G70), H82 (= H93), G141 (= G154), L143 (= L156), N192 (= N205), Y295 (= Y286), R298 (= R289), F343 (= F335), Q429 (= Q425)
6hqfA Structure of phenylalanine ammonia-lyase from petroselinum crispum in complex with (r)-apep
32% identity, 92% coverage: 9:487/518 of query aligns to 30:507/673 of 6hqfA
- active site: Y86 (= Y63), G93 (= G70), Y313 (= Y286), F362 (= F335)
- binding [(1R)-1-amino-2-phenylethyl]phosphonic acid: Y86 (= Y63), F92 (≠ Y69), G178 (= G154), L180 (= L156), N234 (= N205), N346 (= N319), F362 (= F335), E446 (= E421)
6f6tB Phenylalanine ammonia-lyase (pal) from petroselinum crispum complexed with s-appa
32% identity, 92% coverage: 9:487/518 of query aligns to 31:508/677 of 6f6tB
3kdzA X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand (see paper)
33% identity, 96% coverage: 19:514/518 of query aligns to 10:514/527 of 3kdzA
- active site: F53 (≠ Y63), G60 (= G70), H83 (= H93), N193 (= N205), Y296 (= Y286), R299 (= R289), F344 (= F335), Q430 (= Q425)
- binding tyrosine: F53 (≠ Y63), Y59 (= Y69), G60 (= G70), H83 (= H93), G142 (= G154), N193 (= N205), Y296 (= Y286), R299 (= R289), F344 (= F335)
2o7eA Tyrosine ammonia-lyase from rhodobacter sphaeroides (his89phe variant), bound to 2-aminoindan-2-phosphonic acid (see paper)
33% identity, 93% coverage: 19:498/518 of query aligns to 11:498/515 of 2o7eA
- active site: Y54 (= Y63), G61 (= G70), L84 (≠ H93), N195 (= N205), Y292 (= Y286), R295 (= R289), F342 (= F335), Q428 (= Q425)
- binding (2-amino-2,3-dihydro-1h-inden-2-yl)phosphonic acid: Y54 (= Y63), G143 (= G154), L145 (= L156), N195 (= N205), Y292 (= Y286), R295 (= R289), N325 (= N319), F342 (= F335)
Query Sequence
>6939292 FitnessBrowser__SB2B:6939292
MTNQSTEMKETVKFGYGALTIEQVVAIAKGARVELRRDQEYVEYIQRGARFIDSLLAEEG
VVYGVTTGYGDSCTVTVGLDLVHELPLHLSRFHGCGMGRELTPMQSRAVMACRLNSLAIG
KSGVSFELLERIETLINEDICPVIPEEGSVGASGDLTPLSYLAGVLIGERDVFYRGGRLP
SSEVFQKLNITPLKLRPKEGLALMNGTAVMTALACLAYDRADYLTRLSSRITAMASLTLK
GNSNHFDDILFAAKPHPGQSRVASWIRDDLNHHEHPRNSDRLQDRYSIRCAPHIIGVLAD
AQPMLRQFIENELNSANDNPIVDGEGEHILHGGHFYGGHIAFAMDSLKNLVANISDLIDR
QMALVMDPKFNNGLPANLSGAEGARRPINHGFKAVQIGVSAWTAEALKLTMPASVFSRST
ECHNQDKVSMGTIAARDCLRVLELTEQVAAAALLAMTQGMRLRIRQGELCESSLTASVAK
TLAQVSEACPLVTEDRPLEATLRQTLARIQAGEWEVCR
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory